Open AccessIs there a "dolichol recognition sequence" in enzymes that interact with dolichols and other polyisoprenoid substrates?
Author(s) -
John S. Schutzbach
Publication year - 1994
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1994_4715
Subject(s) - dolichol , biochemistry , enzyme , peptide sequence , atp synthase , yeast , amino acid , mannose , biology , chemistry , biosynthesis , gene
Yeast dolichyl-P-mannose synthase and a number of other enzymes that interact with dolichol or dolichyl-P as substrates contain a highly conserved amino-acid sequence that has been proposed as a potential dolichol recognition sequence [Albright, C.F., Orlean, P. & Robbins, P.W. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 7366-7369]. In dolichyl-P-mannose synthase, the most highly conserved amino-acid residues of this domain were modified by site directed mutagenesis, and for one construct the sequence was completely deleted. Enzymes containing the site directed modifications, and the deletion mutant, were found to retain catalytic activity, and all of the modified enzymes had the same apparent affinity for Dol-P as wild type enzyme when assayed in a phospholipid matrix. Based on these results, the amino-acid composition and sequence of the conserved domain are not critically important for the recognition and binding of Dol-P when the synthase is reconstituted in a lipid matrix.